Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy
Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy
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DOI：
10.1021/ja042863o
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发表时间：
2005-04-27
影响因子：
15
通讯作者：
Bodenhausen, G
中科院分区：
文献类型：
--
作者：
Loth, K;Pelupessy, P;Bodenhausen, G
在各向同性溶液中测定了人泛素中不同酰胺键的化学位移各向异性(CSA)张量的主成分和取向，其中包括感兴趣原子核的CSA相互作用和几个偶极-偶极(DID)相互作用。由此得到的CSA参数在一定程度上取决于用于局部运动的模型。考虑了三种情况：受限各向同性扩散，三维高斯轴向涨落(3D-GAF)，以及NHN矢量相对于多肽平面的独立离面运动。
The principal components and orientations of the chemical shift anisotropy (CSA) tensors; of the carbonyl (U), nitrogen (N), and amide proton (H-N) nuclei of 64 distinct amide bonds in human ubiquitin have been determined in isotropic solution by a set of 14 complementary auto- and cross-correlated relaxation rates involving the CSA interactions of the nuclei of interest and several dipole-dipole (DID) interactions. The CSA parameters thus obtained depend to some degree on the models used for local motions. Three cases have been considered: restricted isotropic diffusion, three-dimensional Gaussian axial fluctuations (3D-GAF), and independent out-of-plane motions of the NHN vectors with respect to the peptide planes.